ID A0A0D2GD59_9EURO Unreviewed; 1028 AA.
AC A0A0D2GD59;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|ARBA:ARBA00015856, ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN ORFNames=Z517_09069 {ECO:0000313|EMBL:KIW76625.1};
OS Fonsecaea pedrosoi CBS 271.37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW76625.1, ECO:0000313|Proteomes:UP000053029};
RN [1] {ECO:0000313|EMBL:KIW76625.1, ECO:0000313|Proteomes:UP000053029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW76625.1,
RC ECO:0000313|Proteomes:UP000053029};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in inositol deacylation of GPI-anchored proteins
CC which plays important roles in the quality control and ER-associated
CC degradation of GPI-anchored proteins. {ECO:0000256|ARBA:ARBA00003496,
CC ECO:0000256|RuleBase:RU365011}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the GPI inositol-deacylase family.
CC {ECO:0000256|ARBA:ARBA00006931, ECO:0000256|RuleBase:RU365011}.
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DR EMBL; KN846974; KIW76625.1; -; Genomic_DNA.
DR RefSeq; XP_013280433.1; XM_013424979.1.
DR AlphaFoldDB; A0A0D2GD59; -.
DR STRING; 1442368.A0A0D2GD59; -.
DR GeneID; 25308559; -.
DR VEuPathDB; FungiDB:Z517_09069; -.
DR HOGENOM; CLU_006103_0_0_1; -.
DR OrthoDB; 5477082at2759; -.
DR Proteomes; UP000053029; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR012908; PGAP1-like.
DR InterPro; IPR039529; PGAP1/BST1.
DR PANTHER; PTHR15495:SF7; GPI INOSITOL-DEACYLASE; 1.
DR PANTHER; PTHR15495; NEGATIVE REGULATOR OF VESICLE FORMATION-RELATED; 1.
DR Pfam; PF07819; PGAP1; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU365011};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU365011};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365011};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU365011};
KW Reference proteome {ECO:0000313|Proteomes:UP000053029};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU365011};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU365011};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365011}.
FT TRANSMEM 32..51
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 700..718
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 744..763
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 796..829
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 864..889
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 909..935
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 979..997
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1003..1022
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
SQ SEQUENCE 1028 AA; 114912 MW; C79FC65BF4CAD853 CRC64;
MLLKPKEEVG DSHADTDVRG LRKIRAQSPW TWRPLTLITT AFALLSLAII VRSSLRLQVD
PQGCVMSMMA PTYIKLSGFD TEHSRFATKY SLYLYREEGV DEYTKDNIGL RGAPVLFIPG
NAGSYKQVRS LSSESSRYFH NVLRHDAEAI KAGVRSFDFF TINFNEDLSA FHGQTLLDQA
EYVNEAIAYI LSLYVDSNRI RRDSQLPDPS SVILIGHSMG GIVARTVLVT PKYQANSVNT
IITMSTPHAR PPVSFDADVV SLYQQVNDYW REAYLQRWAS NNPLWHTTLI SIAGGGRDTT
VPSDYTNIAS LVPESHGFTV FSSTIPGVWT AMDHLAITWA DQMRKVIIRS LYDVVDVRRA
AQTKPRVERI KVFRKWFLTG LEDDAPKNMR HAPHEVLLTL GDGTRSAVAK EDNVTIRHFG
VNDHMSAVLL PIPSVDNSTS KIFSLLTDQQ MDDQGGFERM EILFCSAFPL AGGLTSTPLP
IQFDLSPGDP SATRLACKRP AGDAILLPAS TRLSQYPFEQ QPPFTYLTYD LRDLQDHQFV
AMIDKATERS HGWAHAEIVP GADSVVASDV SLPMLLLRGL NLELPSNRPL VTEIRVPSIR
SSLLAYTLQI RQHGCTTDTE LFTPLLRQHI DSPYESKYFV NFKQGDVNLH GVAPFMPPTL
DGRESKAGVA FQIWSDPTCN SSLEIRLRAD PVGSLGKLVI RYRTVFAVFP LLVVAMVLRK
QFRVYDNSGV FISFSESLDQ SLRLPLPVLM LSMTFFATAF TTASSANLVS SSPAQTNGTV
VDFAQNDLLL GSQDTFFWFL VPLAGLLSVG ACVLINYAVL GLLHFIVIVS NFVSQRYMKP
DDGDKVMTPG FVASTPRRRA INTAVLLFLV ATIIPYPFAY VVACIVQVFT CARALRHAKD
SRSGPAHNFF NYTYSILILM LWVLPINLPV LVVWIHNLAV HWLTPFSSHH NVLSIMPFIL
LVETLSSGKM VPSVRSFRWA TNLLFFVLAV YAALYGMTYA YRLHYIANII ALWLVLLHFS
TYQKRIPT
//
